Results 31 to 40 of about 4,908 (204)

The IMPORTance of the Nucleus during Flavivirus Replication

Viruses, 2017
Flaviviruses are a large group of arboviruses of significant medical concern worldwide. With outbreaks a common occurrence, the need for efficient viral control is required more than ever.
Adam J. Lopez-Denman, Jason M. Mackenzie
doaj   +1 more source

Targeting nuclear transporters in cancer: Diagnostic, prognostic and therapeutic potential [PDF]

, 2016
The Karyopherin superfamily is a major class of soluble transport receptors consisting of both import and export proteins. The trafficking of proteins involved in transcription, cell signalling and cell cycle regulation among other functions across the ...
Aggarwal, Albee, Alnabulsi, Alshareeda, Altan, Angus, Behrens, Bernis, Blower, Brinkmann, Brinkmann, Cansizoglu, Chang, Christiansen, Dahl, Das, Dasso, Depping, Dikovskaya, Forbes, Gluz, Gontan, Gorlich, Gousias, Gousias, Gousias, Grupp, Gruss, Hashimoto, Hintersteiner, Hu, Huang, Huang, Huang, Hutchins, Hügel, Ishizawa, Jensen, Jiang, Kahle, Kau, Kazim, Kim, Kimura, King, Knauer, Kojima, Kosugi, Kudo, Kurisaki, Kutay, Kuusisto, Kuusisto, Lapalombella, Latvia, Lau, Laurila, Li, Liang, Liao, Lin, Lin, Lorenzato, Ma, Marfori, Martens-de Kemp, Melo, Mortezavi, Mosammaparast, Muller, Nevins, Noske, Parikh, Poon, Pumroy, Quan, Quensel, Rensen, Sakai, Scherf, Shen, Shi, Shiraki, Sillje, Smith, Smith, Soderholm, Song, Stawerski, Stella Tsai, Stewart, Tai, Torgerson, Turner, Turner, Wagstaff, Wang, Wang, Wang, Watt, Watt, Watt, Wellmann, Wiese, Winkler, Winnepenninckx, Wu, Yan, Yang, Yao, Yoshitake, Yu, Zender, Zheng, Zhou, Zhu, Zhu, Zienkiewicz   +117 more
core   +1 more source

Adjunct Duties for Karyopherins: Regulating Septin Sumoylation [PDF]

Developmental Cell, 2007
Karyopherins are shuttling transport receptors regulated by the small GTPase Ran, which move cargo between the nucleus and cytoplasm by passing through the nuclear pore complexes. A recent paper in Journal of Cell Biology (Makhnevych et al., 2007) highlights an additional role for karyopherins during mitosis, in regulating the sumoylation status of the
Panse, Vikram Govind, Hurt, Ed
openaire   +2 more sources

HIV-1 Vpr antagonizes innate immune activation by targeting karyopherin-mediated NF-κB/IRF3 nuclear transport

eLife, 2020
HIV-1 must replicate in cells that are equipped to defend themselves from infection through intracellular innate immune systems. HIV-1 evades innate immune sensing through encapsidated DNA synthesis and encodes accessory genes that antagonize specific ...
Hataf Khan, Rebecca P Sumner, Jane Rasaiyaah, Choon Ping Tan, Maria Teresa Rodriguez-Plata, Chris Van Tulleken, Douglas Fink, Lorena Zuliani-Alvarez, Lucy Thorne, David Stirling, Richard SB Milne, Greg J Towers   +11 more
doaj   +1 more source

Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis [PDF]

, 2013
The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes
Ausubel FM, Boulon S, Boulon S, Burns N, Chook YM, Cingolani G, Cook AG, Cramer P, Czeko E, Edwards AM, Estruch F, Forget D, Garí E, Gavin AC, Giaever G, Graumann J, Görlich D, Imasaki T, Juanes MA, Kakihara Y, Kimura M, Krogan NJ, Lau D, Neville M, Pascual-García P, Peiró-Chova L, Peiró-Chova L, Pemberton LF, Reyes-Pardo H, Soriano-Carot M, Staresincic L, Strahm Y, Te J, Watanabe M, Wild T, Zhao R, Zhao R   +36 more
core   +1 more source

Cloning and characterization of human karyopherin β3 [PDF]

Proceedings of the National Academy of Sciences, 1997
Nuclear import of classical nuclear localization sequence-bearing proteins is mediated by karyopherin α/β1 heterodimers. A second nuclear import pathway, mediated by karyopherin β2 (transportin), recently was described for mRNA-binding proteins. Here we report the cloning and characterization of human karyopherin β3, which may be involved in a third ...
N R, Yaseen, G, Blobel
openaire   +2 more sources

The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence. [PDF]

Proceedings of the National Academy of Sciences, 1996
By using proteolysis, recombinant mutant proteins, or synthetic peptides and by testing these reagents in liquid phase binding or nuclear import assays, we have mapped binding regions of karyopherin alpha. We found that the C-terminal region of karyopherin alpha recognizes the nuclear localization sequence (NLS), whereas its N-terminal region binds ...
J, Moroianu, G, Blobel, A, Radu
openaire   +2 more sources

IPO5 promotes the proliferation and tumourigenicity of colorectal cancer cells by mediating RASAL2 nuclear transportation

Journal of Experimental & Clinical Cancer Research, 2019
Background Karyopherin nuclear transport receptors play important roles in tumour development and drug resistance and have been reported as potential biomarkers and therapeutic targets for tumour treatment.
Wenjuan Zhang, Yanxia Lu, Xiaomin Li, Jianming Zhang, Weihao Lin, Wei Zhang, Lin Zheng, Xuenong Li   +7 more
doaj   +1 more source

Karyopherin α 3 and Karyopherin α 4 Proteins Mediate the Nuclear Import of Methyl-CpG Binding Protein 2 [PDF]

Journal of Biological Chemistry, 2015
Methyl-CpG binding protein 2 (MeCP2) is a nuclear protein with important roles in regulating chromatin structure and gene expression, and mutations in MECP2 cause Rett syndrome (RTT). Within the MeCP2 protein sequence, the nuclear localization signal (NLS) is reported to reside between amino acids 255-271, and certain RTT-causing mutations overlap with
Steven Andrew, Baker, Laura Marie, Lombardi, Huda Yahya, Zoghbi   +2 more
openaire   +2 more sources

The HIV capsid mimics karyopherin engagement of FG-nucleoporins. [PDF]

Nature
AbstractHIV can infect non-dividing cells because the viral capsid can overcome the selective barrier of the nuclear pore complex and deliver the genome directly into the nucleus1,2. Remarkably, the intact HIV capsid is more than 1,000 times larger than the size limit prescribed by the diffusion barrier of the nuclear pore3. This barrier in the central
Dickson CF, Hertel S, Tuckwell AJ, Li N, Ruan J, Al-Izzi SC, Ariotti N, Sierecki E, Gambin Y, Morris RG, Towers GJ, Böcking T, Jacques DA.   +12 more
europepmc   +4 more sources